Search: 1000 results found for "Prolactin PRL"

Description:

Myelin Protein Zero-Like 1 Human Recombinant

Myelin Protein Zero-Like 1, PZRa, PZR, Protein Zero-Related, PZRb, Immunoglobulin Family Transmembrane Protein, Myelin Protein Zero-Like Protein 1, MPZL1b, Protein Zero Related, PZR1b.

Product # :

PRO-1611

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Description

MPZL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (38-162) and having a molecular mass of 16.1kDa.MPZL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MPZL1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Myelin Protein Zero-Like 1 (MPZL1) is a cell surface receptor, which is involved in signal transduction processes. MPZL1 recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. MPZL1 is a main receptor for concanavalin-A (ConA) and it is involved in cellular signaling induced by ConA, which most likely includes Src family tyrosine-protein kinases. MPZL1 Isoform 3 appears to have a dominant negative role by blocking tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, might be involved in regulation of integrin-mediated cell motility.
Synonyms
Myelin Protein Zero-Like 1, PZRa, PZR, Protein Zero-Related, PZRb, Immunoglobulin Family Transmembrane Protein, Myelin Protein Zero-Like Protein 1, MPZL1b, Protein Zero Related, PZR1b.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLEVYTPK EIFVANGTQG KLTCKFKSTS TTGGLTSVSW SFQPEGADTT VSFFHYSQGQ VYLGNYPPFK DRISWAGDLD KKDASINIEN MQFIHNGTYI CDVKNPPDIV VQPGHIRLYV VEKENLPV.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Calmodulin Like 3 Human Recombinant

Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.

Product # :

PRO-1323

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Description

CALML3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-149 a.a.) and having a molecular mass of 19kDa.CALML3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CALML3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Calmodulin Like 3 (CALML3) is a member of the calmodulin family and contains 4 EF-hand domains. The CALML3 protein may be similar to that of genuine calmodulin and may in fact compete with calmodulin by binding, with different affinities, to cellular substrates. CALML3 protein is expressed in normal mammary, prostate, cervical, and epidermal tissues.
Synonyms
Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMADQLT EEQVTEFKEA FSLFDKDGDG CITTRELGTV MRSLGQNPTE AELRDMMSEI DRDGNGTVDF PEFLGMMARK MKDTDNEEEI REAFRVFDKD GNGFVSAAEL RHVMTRLGEK LSDEEVDEMI RAADTDGDGQ VNYEEFVRVL VSK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Myeloid Cell Leukemia Sequence 1 Human Recombinant

Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.

Product # :

PRO-1202

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Description

MCL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (1-327) and having a molecular mass of 37.2 kDa.MCL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The MCL1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.
Synonyms
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR TKRDWLVKQR GWDGFVEFFH VEDLEGG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Galectin-8 Human Recombinant, His Tag

Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

Product # :

CYT-727

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SDS-PAGE

Description

LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-317 a.a.) and having a molecular mass of 37.9 kDa. The LGALS8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.

SDS-PAGE

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Introduction
LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.
Synonyms
Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.
Background
What is the molecular weight/Mw of LGALS8 HUMAN, HIS Protein?
LGALS8 HUMAN, HIS Protein has a total Mw of 37.9kDa.

What is the source or expression system of LGALS8 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of LGALS8 HUMAN, HIS Protein?
LGALS8 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS8 HUMAN, HIS Protein?
The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.What is the amino acid
sequence of LGALS8 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

What applications can LGALS8 HUMAN, HIS Protein be used in?
LGALS8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS8 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS8 HUMAN, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Humanin

Product # :

HOR-042

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Description

Humanin Synthetic is a single, non-glycosylated polypeptide chain containing 24 amino acids, having a molecular mass of 2687 Dalton and a Molecular formula of C119H204N34O32S2 .

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Humanin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Humanin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Humanin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.
Background
Humanin, a small peptide derived from the mitochondrial genome, has emerged as a remarkable molecule with diverse cellular protective functions. This research paper aims to provide a comprehensive analysis of Humanin, exploring its biochemical properties, mechanisms of action, and potential therapeutic applications in various disease contexts.
Humanin, initially discovered for its role in neuroprotection, has since garnered interest for its broad spectrum of cytoprotective effects. Derived from the mitochondrial 16S ribosomal RNA, this small peptide plays a critical role in safeguarding cells from various stressors (Harvey, 2008). This paper delves into the complexities of Humanin, uncovering its multifaceted nature and potential clinical applications.
Humanin is a 24-amino acid peptide with a unique secondary structure that contributes to its cellular protective functions. It localizes to both the cytoplasm and mitochondria, where it interacts with various proteins involved in apoptotic and oxidative stress pathways (Hoang et al., 2019). Additionally, Humanin can undergo post-translational modifications, further diversifying its actions.
Humanin exerts its protective effects through multiple mechanisms. It interacts with the pro-apoptotic protein Bax, inhibiting its translocation to the mitochondria and preventing the release of cytochrome c (Hashimoto et al., 2001). Humanin also modulates the activities of caspases, key mediators of cell death pathways, thereby promoting cell survival in stressful conditions (Nakagawa et al., 2002).
Beyond its initial recognition as a neuroprotective agent, Humanin has demonstrated cytoprotective effects in various cell types, including cardiomyocytes, neurons, and endothelial cells (Chai et al., 2019). It attenuates oxidative stress, reduces mitochondrial dysfunction, and promotes cell viability, thereby safeguarding cells from a multitude of insults.
The multifaceted protective functions of Humanin offer promising therapeutic potential in various disease contexts. Research has shown its efficacy in mitigating neurodegenerative disorders, cardiovascular diseases, and age-related pathologies (Muzumdar et al., 2009). Furthermore, Humanin's ability to attenuate inflammation and promote tissue repair opens new avenues for therapeutic interventions.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Oxyntomodulin Porcine Recombinant

Product # :

HOR-292

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Description

Oxyntomodulin Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4420.86 Dalton. The OXM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
OXM a 37 amino acid peptide which contains the glucagon sequence extended by a C-terminal basic octapeptide, its primary structure is identical in all mammals except in pig and cattle. OXM is released from the gut during digestion, together with glicentin another octapeptide containing molecule. It is considered as a putative physiological regulator of gastric acid secretion, it inhibits histamine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oxyntomodulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OXM should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Oxyntomodulin in 20mM acetic acid.
Amino Acid Sequence
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fertirelin

Product # :

HOR-037

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Description

Fertirelin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1153.31 Dalton and a Molecular formula of C55H76N16O12.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Fertirelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fertirelin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Fertirelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.
Background
Fertirelin, a potent gonadotropin-releasing hormone (GnRH) analogue, is crucial for fertility regulation in animals. This research paper endeavors to expound on the biochemical attributes of fertirelin and its potential therapeutic applications in veterinary medicine.
Fertirelin, a synthetic analogue of the natural gonadotropin-releasing hormone, plays a fundamental role in fertility regulation in veterinary medicine. It stimulates the secretion of luteinizing hormone and follicle-stimulating hormone, crucial for reproduction (Kotwica et al., 2005). This paper aims to delve into the biochemical characteristics of fertirelin and its potential applications.
Fertirelin, as a GnRH analogue, elicits its action by binding to GnRH receptors located on pituitary gonadotroph cells. This leads to the release of luteinizing hormone and follicle-stimulating hormone, key players in ovulation and spermatogenesis (Kotwica et al., 2005).
In the realm of veterinary medicine, fertirelin is primarily used for treating ovarian follicular cysts in dairy cattle (Bosu & Peter, 1987). Its potent stimulatory effect on gonadotropin secretion facilitates ovulation and contributes to fertility management strategies.
The potential of fertirelin extends beyond the current applications. Further research into the precise mechanism of action and potential side effects can enhance its utilization. Overall, fertirelin presents a powerful tool in veterinary reproductive medicine, making it a focal point of interest for future studies.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Placental Growth Factor Human Recombinant

PIGF, PGF, PLGF-1

Product # :

CYT-1193

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Description

PLGF Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-170) containing 160 amino acids and having a molecular mass of 18.3kDa.PLGF is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

PLGF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Placental Growth Factor (PLGF) which is a member of the VEGF sub-family, is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. PLGFmainly plays a role in trophoblast growth and differentiation and binds to receptor vegfr-1/flt1.
Synonyms
PIGF, PGF, PLGF-1
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSMAVPPQQ WALSAGNGSS EVEVVPFQEV WGRSYCRALE RLVDVVSEYP SEVEHMFSPS CVSLLRCTGC CGDENLHCVP VETANVTMQL LKIRSGDRPS YVELTFSQHV RCECRPLREK MKPERRRPKG RGKRRREKQR PTDCHLCGDA VPRRHHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

DiGeorge Syndrome Critical Region Gene 6-Like Human Recombinant

Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.

Product # :

PRO-1454

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Description

DGCR6L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27.3kDa.DGCR6L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DGCR6L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 1mM DTT and 250mM Imidazole.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
DiGeorge syndrome critical region 6-like protein (DGCR6L) shares homology with the Drosophila gonadal protein, it is expressed in gonadal tissues and germ cells, and with the human laminin gamma-1 chain which functions in cell attachment and migration. DGCR6L is located in a region of chromosome 22 involved in the DiGeorge syndrome, one aspect of a wider collection of anomalies referred to as the CATCH 22 syndrome. Moreover, it is one of two functional genes encoding nearly identical proteins which have analogous expression patterns.
Synonyms
Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMERYAAA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVVQA AQQRELEAVE HRIREEQRAM DQKIILELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCRAGNAA LGLGGPWQSP AAQCDQKGSP VPP.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Progastricsin-C Human Recombinant

Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

Product # :

ENZ-966

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Description

PGC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (17-388 a.a.) and having a molecular mass of 41.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PGC is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

PGC protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.
Synonyms
Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
AVVKVPLKKF KSIRETMKEK GLLGEFLRTH KYDPAWKYRF GDLSVTYEPM AYMDAAYFGE ISIGTPPQNF LVLFDTGSSN LWVPSVYCQS QACTSHSRFN PSESSTYSTN GQTFSLQYGS GSLTGFFGYD TLTVQSIQVP NQEFGLSENE PGTNFVYAQF DGIMGLAYPA LSVDEATTAM QGMVQEGALT SPVFSVYLSN QQGSSGGAVV FGGVDSSLYT GQIYWAPVTQ ELYWQIGIEE FLIGGQASGW CSEGCQAIVD TGTSLLTVPQ QYMSALLQAT GAQEDEYGQF LVNCNSIQNL PSLTFIINGV EFPLPPSSYI LSNNGYCTVG VEPTYLSSQN GQPLWILGDV FLRSYYSVYD LGNNRVGFAT AALEHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Follistatin Like 1 Human Recombinant

Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.

Product # :

CYT-792

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sds-page

Description

FSTL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 309 amino acids (21-308) and having a molecular mass of 34.9 kDa.FSTL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The FSTL1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
FSTL1 protein resembles follistatin, an ACTV-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.
Background
What is the molecular weight/Mw of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein has a total Mw of 34.9kDa.

What is the source or expression system of FSTL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of FSTL1 HUMAN Protein?
FSTL1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FSTL1 HUMAN Protein?
The biological functionality of FSTL1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of FSTL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MEEELRSKSK ICANVFCGAG RECAVTEKGE PTCLCIEQCK PHKRPVCGSN GKTYLNHCEL HRDACLTGSK IQVDYDGHCK EKKSVSPSAS PVVCYQSNRD ELRRRIIQWL EAEIIPDGWF SKGSNYSEIL DKYFKNFDNG DSRLDSSEFL KFVEQNETAI NITTYPDQEN NKLLRGLCVD ALIELSDENA DWKLSFQEFL KCLNPSFNPP EKKCALEDET YADGAETEVD CNRCVCACGN WVCTAMTCDG KNQKGAQTQT EEEMTRYVQE LQKHQETAEK TKRVSTKEI.

What applications can FSTL1 HUMAN Protein be used in?
FSTL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FSTL1 HUMAN Protein?
The endotoxin level is minimal, FSTL1 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Parathyroid Hormone Related Protein N15 Labeled Human Recombinant

Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.

Product # :

HOR-005

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Description

PTHrP N15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids, having an MW of 10033 Da labeled by the stable isotope N15.The PTHrP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PthRp N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS,
pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
PTHrP is a powerful and discriminating agonist of PTH2R which takes part in adenyl cyclase activation and intracellular calcium levels elevation. PTHrP encourages protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. Additionally, PTHrP inhibits cell proliferation through its contribution to PTH2R activation, activates nociceptors and nociceptive circuits and acts as a neuropeptide in spermatogenesis.
Synonyms
Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PTHrP N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTHrP N15 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Inhibin Alpha Human Recombinant

Product # :

HOR-303

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Description

Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE analysis.

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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
Amino Acid Sequence
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Soluble RANK Ligand Human Recombinant, His Tag

Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

Product # :

CYT-692

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Description

sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (140-317 a.a) and having a molecular mass of 22.3kDa.sRANKL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

sRANKL protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIRAEKAMVD GSWLDLAKRS KLEAQPFAHL TINATDIPSG SHKVSLSSWY HDRGWAKISN MTFSNGKLIV NQDGFYYLYA NICFRHHETS GDLATEYLQL MVYVTKTSIK IPSSHTLMKG GSTKYWSGNS EFHFYSINVG GFFKLRSGEE ISIEVSNPSL LDPDQDATYF GAFKVRDID.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Adipotide

Product # :

HOR-060

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Description

Adipotide is a synthetic single, non-glycosylated polypeptide chain containing 25 amino acids, having a molecular mass of 2555 Dalton and a Molecular formula of C111H204N36O28S2.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Adipotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Adipotide should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Adipotide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Cys-Lys-Gly-Gly-Arg-Ala-Lys-AspCys-Gly-Gly-d-Lys-d-Leu-d-Ala-d-Lys-d-Leu-d-Ala-d-Lys-d-Lys-d-Leud-Ala-d-Lys-d-Leu-d-Ala-d-Lys-OH (disulfide bond).
Background
Adipotide is a proapoptotic peptidomimetic which selectively destroy the blood vessels supplying white adipose tissue. Adipotide plays a main role in translational metabolic research. Adipotide is the most potent proof-of-concept for non-hormonal, vascular-targeted fat reduction.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant

PK1, PRK1, Prokineticin 1, EG-VEGF.

Product # :

CYT-338

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Description

EG-VEGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa. The EG-VEGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

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Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
Synonyms
PK1, PRK1, Prokineticin 1, EG-VEGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.
Background
Title: Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant: Insights into its Role in Endocrine Disorders and Therapeutic Applications
Abstract:

Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a unique angiogenic factor that plays a crucial role in the development and function of endocrine glands. This research paper provides a comprehensive analysis of human recombinant EG-VEGF, focusing on its production, characterization, and potential applications in endocrine disorders. The paper highlights the significance of EG-VEGF in endocrine gland angiogenesis and explores its role in the pathogenesis of endocrine-related diseases. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EG-VEGF in endocrine disorders and related conditions. The information presented in this paper aims to enhance our understanding of human recombinant EG-VEGF and its utility as a research tool and a potential therapeutic agent.
Introduction:

Endocrine Gland Vascular Endothelial Growth Factor (EG-VEGF) is a growth factor specifically expressed in endocrine tissues. Human recombinant EG-VEGF, produced through genetic engineering techniques, offers a valuable tool for studying its angiogenic properties and exploring its potential therapeutic applications in endocrine disorders.
Production and Characterization:

Recombinant EG-VEGF is typically generated using mammalian cell expression systems. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EG-VEGF.
Role in Endocrine Disorders:

EG-VEGF is involved in the regulation of endocrine gland angiogenesis, which is critical for their development, hormone secretion, and overall function. Dysregulation of EG-VEGF signaling has been implicated in various endocrine disorders, including preeclampsia, gestational trophoblastic diseases, and adrenal disorders. Recombinant EG-VEGF serves as a valuable tool for investigating the mechanisms underlying EG-VEGF-mediated angiogenesis and its potential implications in endocrine-related diseases.
Therapeutic Implications:

Manipulation of angiogenesis holds promise as a therapeutic approach in various endocrine disorders. Recombinant EG-VEGF offers potential therapeutic applications in promoting neovascularization and restoring endocrine gland function. Ongoing research and clinical trials are investigating the therapeutic potential of recombinant EG-VEGF in conditions such as hypopituitarism, ovarian disorders, and other endocrine-related pathologies.
Conclusion:

Human recombinant EG-VEGF represents a valuable research tool and a potential therapeutic agent. Its production, characterization, and applications in endocrine disorders contribute to our understanding of endocrine gland angiogenesis and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EG-VEGF offer promising avenues for improving outcomes in endocrine disorders and related conditions.
What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.7kDa.

What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.

What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EG-VEGF Protein?
The activity as determined by the dose-dependent proliferation of MIA PaCa-2 cells is typically 1-4 μg/ml.

What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF.

What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Prefoldin Subunit 6 Human Recombinant

Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.

Product # :

PRO-178

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Description

PFDN6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-129a.a.) and having a molecular mass of 16.7 kDa. PFDN6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PFDN6 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PFDN6 is a subunit of the heteromeric prefoldin complex that chaperones developing actin and alpha- and beta-tubulin chains until they are transferred to the cytosolic chaperonin containing TCP1 (CCT) complex. PFDN6 binds specifically to cytosolic chaperonin (c-CPN), transfers target proteins to it and bind to developing polypeptide chain to promote folding in a setting where there are many competing pathways for nonnative proteins.
Synonyms
Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA AKAGAPGKA

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thyrostimulin Alpha Human Recombinant

GPA2, GPHA2, ZSIG51, Glycoprotein hormone alpha-2, MGC126572.

Product # :

HOR-258

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Quantity :

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Shipped at Room temp

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Description

GPHA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a total molecular mass of 13.28 kDa. The Thyrostimulin contains His tag which consists of 14 additional amino acids.The amino acid sequence of the recombinant human Thyrostimulin beta subunit is 100% homologous to the amino acid sequence of the human Thyrostimulin beta subunit without signal sequence. (N-terminal 24AA).Thyrostimulin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GPHA2 filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH 4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Human thyrostimulin ranks among the glycoprotein hormone family. These hormones consist of two subunits, the common alpha- and specific beta-subunits, which associate noncovalently to form a heterodimer. The alpha-subunit combines with four distinct beta-subunits giving rise to four biologically active hormones in human: FSH, LH, TSH, and CG. FSH, LH, and TSH, mainly expressed in the anterior pituitary, are essential for coordinated endocrine regulation in the hypothalamus- pituitary axis and show to activate specific G protein–coupled receptors in the thyroid (TSH receptor) and gonads (LH and FSH receptors), respectively.
The heterodimeric glycoprotein hormones have only been identified in vertebrates and are highly conserved in organisms from primitive rayfin fish (Chondrostei) to human in both primary sequences and functional characteristics.
Corticotroph-derived glycoprotein hormone (CGH), also referred to as thyrostimulin, is a noncovalent heterodimer of glycoprotein hormone alpha 2 (GPHA2) and glycoprotein hormone beta 5 (GPHB5).
Recombinant A2/B5 heterodimeric glycoproteins activates human TSH receptors, but not LH and FSH receptors, and shows high affinity to TSH receptors in a radioligand receptor assay. The heterodimer also stimulates cAMP production and thymidine incorporation by cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo. This new heterodimeric glycoprotein hormone was named as thyrostimulin based on its thyroid-stimulating activity. The expression of thyrostimulin in the anterior pituitary known to express TSH receptors suggested a paracrine mechanism.
Synonyms
GPA2, GPHA2, ZSIG51, Glycoprotein hormone alpha-2, MGC126572.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thyrostimulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GPHA2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of ~ 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MRGSHHHHHH GMAS QEAVIPG CHLHPFNVTV RSDRQGTCQG SHVAQACVGH CESSAFPSRY SVLVASGYRH NITSVSQCCT ISGLKKVKVQ LQCVGSRREE LEIFTARACQCDMCRLSRY.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

C-Peptide

Product # :

HOR-046

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formulation
purity
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Description

C-Peptide Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3020 Dalton and a Molecular formula of C129H211N35O48S .

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized C-Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution C-Peptide should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized C-Peptide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Glu-Ala-Glu-Asp-Leu-Gln-Val-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Pro-Gly-Ala-Gly-Ser-Leu-Gln-Pro-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-OH.
Background
C-peptide, a small peptide derived from proinsulin, has garnered increasing attention in recent years for its multifaceted physiological functions and clinical significance, particularly in the context of diabetes mellitus. While initially considered a mere byproduct of insulin synthesis, research has revealed that C-peptide exerts unique biological effects, extending beyond glycemic control. This research endeavors to comprehensively investigate the roles of C-peptide, shedding light on its diverse functions and potential applications in diabetes management and other areas of healthcare.
The primary objective of this study is to unravel the mechanisms underlying the physiological actions of C-peptide. In vitro experiments using cellular and tissue models will be conducted to explore how C-peptide interacts with cellular receptors and signaling pathways. This includes investigations into its influence on insulin secretion, glucose uptake, and endothelial function. Understanding these mechanisms is essential for delineating the potential therapeutic applications of C-peptide.
The second objective is to assess the clinical relevance of C-peptide in diabetes management. Clinical trials involving individuals with type 1 and type 2 diabetes will be conducted to evaluate the effects of exogenous C-peptide administration on glycemic control, insulin sensitivity, and microvascular complications. These studies may provide valuable insights into the use of C-peptide as an adjunct therapy in diabetes treatment.
The third objective is to explore the broader implications of C-peptide in healthcare. Research will investigate the potential role of C-peptide in conditions beyond diabetes, such as its effects on cardiovascular health, neuroprotection, and wound healing. Understanding the multifunctional properties of C-peptide may open up new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of C-peptide, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may lead to innovative approaches for diabetes management and offer insights into the broader healthcare implications of C-peptide.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Agouti–Related Protein Human Recombinant

ART, AGRT, ASIP2, MGC118963, AGRP.

Product # :

HOR-283

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Quantity :

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Description

The Human Agouti-related protein is created as a recombinant protein with N-terminal fusion of His Tag.The Human Agouti-related protein His-Tagged Fusion Protein, produced in E. coli, is 14.4 kDa (calculated) protein containing 112 amino acid residues of the human AGRP and 16 additional amino acid residues - His Tag, thrombin cleavage site (highlighted).The AGRP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AGRP protein was lyophilized from 0.5mg/ml in 5mM TRIS, 25mM NaCl, pH 7.5.

Purity

Purity of Agouti–related protein recombinant human is >95% as determined by SDS-PAGE.

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Introduction
Agouti-related protein is an endogenous antagonist of hypothalamic alpha-melanocortin receptors MC3R and MC4R with potent orexigenic activity. Although a complete deletion of the AGRP gene does not produce any significant metabolic phenotypes, reduction in AGRP expression by RNA interference is associated with increased metabolic rate along with reduced weight gain. In hypothalamus, it is produced by neurons in the medial portion of arcuate nucleus, which produce also the potent orexigenic peptide Neuropeptide Y (NP-Y). Another site of central AGRP production is the hypothalamic nucleus. AGRP encompasses 132 amino acid residues and its alpha-melanocortin inhibiting activity results in a 34 amino acid cystine knot domain within the C-terminal (87-132) portion of the protein. Both AGRP and NP-Y expression was shown to be suppressed by leptin. Central administration of AGRP induces hyperphagia and increased gain in body weight in rodents, but may also exert metabolic effects even when hyperphagia is prevented. In the absence of hyperphagia, intracerebralventricular administration of AGRP caused significant increases in plasma leptin and insulin concentrations (twofold and 1.5-fold, respectively) and fat pad mass.
In the periphery, AGRP mRNA was found in adrenal glands, lung, testis, ovary, skeletal muscle and adipose tissue in humans or rodents. In the adrenals, it was shown that AGRP antagonizes glucosteroid production mediated by MC4R. AGRP could then modulate locally the functions of some peripheral tissues such as adrenals.
In human and rat serum, detectable levels of AGRP-like activity were reported in the lower picogram range. The serum AGRP levels were elevated in obese humans compared to lean controls and increased with fasting in rats.
Synonyms
ART, AGRT, ASIP2, MGC118963, AGRP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized AGRP protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MKHHHHHHHM LVPRGSAQMG LAPMEGIRRP DQALLPELPG LGLRAPLKKT TAEQAEEDLL QEAQALAEVL DLQDREPRSS RRCVRLHESC LGQQVPCCDP CATCYCRFFN AFCYCRKLGT AMNPCSRT.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Selectin P Ligand Human Recombinant

Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.

Product # :

PRO-2714

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Description

SELPLG Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 496 amino acids (42-295 a.a) and having a molecular mass of 53.4kDa.SELPLG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The SELPLG solution (1mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SELPLG glycoprotein functions as a high affinity counter-receptor for the cell adhesion selectin molecules (P, E and L) located in stimulated T lymphocytes and myeloid cells. SELPLG binds leukocytes to activated platelets or endothelia expressing selectins, a vital role in leukocyte trafficking throughout inflammation. In order to have a high-affinity binding activity SELPLG needs two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. Polymorphisms and abnormal expression of SELPLG are linked to defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.
Synonyms
Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSQATEYEY LDYDFLPETE PPEMLRNSTD TTPLTGPGTP ESTTVEPAAR RSTGLDAGGA VTELTTELAN MGNLSTDSAA MEIQTTQPAA TEAQTTPLAA TEAQTTRLTA TEAQTTPLAA TEAQTTPPAA TEAQTTQPTG LEAQTTAPAA MEAQTTAPAA MEAQTTPPAA MEAQTTQTTA MEAQTTAPEA TEAQTTQPTA TEAQTTPLAA MEALSTEPSA TEALSMEPTT KRGLFIPFSV SSVTHKGIPM AASNLSVLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Mitochondrial Ribosomal Protein L1 Human Recombinant

BM022, L1MT, MRP-L1, 39S ribosomal protein L1, mitochondria, MRPL1.

Product # :

PRO-1431

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Description

MRPL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (51-325) and having a molecular mass of 33.8kDa. MRPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The MRPL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Mitochondrial Ribosomal Protein L1 (MRPL1) exists as a component of the 39S ribosomal subunit and operates in conjunction with other MRPs to mediate protein synthesis. Mitochondrial ribosomes consist of a large 39S subunit and a small 28S subunit, both of which are consist of multiple mitochondrial ribosomal proteins (MRPs) that are encoded by nuclear genes and are vital for protein synthesis within mitochondria. MRPL1 exists as 2 isoforms produced by alternative splicing. Isoform 1 of MRPL1 is ubiquitously expressed while isoform 2 is particularly expressed in heart.
Synonyms
BM022, L1MT, MRP-L1, 39S ribosomal protein L1, mitochondria, MRPL1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKKTKKGA KEKTPDEKKD EIEKIKAYPY MEGEPEDDVY LKRLYPRQIY EVEKAVHLLK KFQILDFTSP KQSVYLDLTL DMALGKKKNV EPFTSVLSLP YPFASEINKV AVFTENASEV KIAEENGAAF AGGTSLIQKI WDDEIVADFY VAVPEIMPEL NRLRKKLNKK YPKLSRNSIG RDIPKMLELF KNGHEIKVDE ERENFLQTKI ATLDMSSDQI AANLQAVINE VCRHRPLNLG PFVVRAFLRS STSEGLLLKI DPLLPKEVKN EESEKEDA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Mitochondrial Ribosomal Protein L28 Human Recombinant

MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.

Product # :

PRO-1279

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Description

MRPL28 Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (56-256) and having a molecular mass of 25.8 kDa. MRPL28 is fused to 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The MRPL28 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.5), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
MRPL28 is found in a variety of normal tissues such as spleen, testis, thymus, liver, kidney, brain, adrenal, lung and retinal tissue. 39S ribosomal protein L28, mitochondrial (MRPL28), is a part of the ribosomal protein L28P family. Mammalian mitochondrial ribosomal proteins encoded by nuclear genes and helps in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL28 is an important therapeutic reagent for HLA-A24 (A24) patients since this antigen is distinguished by tumor-infiltrating lymphocyte (TIL) 1290, which targets the A24 serotype.
Synonyms
MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNGQRERVED VPIPIYFPPE SQRGLWGGEG WILGQIYANN DKLSKRLKKV WKPQLFEREF YSEILDKKFT VTVTMRTLDL IDEAYGLDFY ILKTPKEDLC SKFGMDLKRG MLLRLARQDP QLHPEDPERR AAIYDKYKEF AIPEEEAEWV GLTLEEAIEK QRLLEEKDPV PLFKIYVAEL IQQLQQQALS EPAVVQKRAS GQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant

FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.

Product # :

ENZ-338

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Description

SlyD Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids and having a molecular mass of 21 kDa.

Source

Escherichia Coli.

Formulation

SlyD protein solution contains 20mM Tris pH-7.5.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

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Introduction
SlyD accessiton#: NP_755987 is a putative folding helper protein from the Escherichia coli cytosol, which has N-terminal prolyl isomerase domain of the FKBP type and a most likely unstructured C-terminal tail. SlyD is an important factor in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.
Synonyms
FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase, SlyD.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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